Comprehensive study on the structure of the BSA from extended-to aged form in wide (2-12) pH range
In this work we studied the structure of the bovine serum albumin (BSA) and the protein-ligand interactions since researchers prefer to use them as carriers in drug delivery systems. Systematic study (between pH 2-12, in double distilled water and physiological salt solution) was carried out to dete...
Elmentve itt :
| Szerzők: | |
|---|---|
| Dokumentumtípus: | Cikk |
| Megjelent: |
Elsevier
2016
|
| Sorozat: | INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
88 |
| doi: | 10.1016/j.ijbiomac.2016.03.030 |
| mtmt: | 3149928 |
| Online Access: | http://publicatio.bibl.u-szeged.hu/12125 |
| Tartalmi kivonat: | In this work we studied the structure of the bovine serum albumin (BSA) and the protein-ligand interactions since researchers prefer to use them as carriers in drug delivery systems. Systematic study (between pH 2-12, in double distilled water and physiological salt solution) was carried out to determine the changes in the secondary and the tertiary structures of the BSA, the apparent molecular weight (M-w), the size (d(LS)) and the electrokinetic potential (zeta). At pH 7, the BSA has higher stability in the absence (zeta = -69 mV, d(LS) =2.2 nm, A(2) = 1.4 x 10(-3) mlmol/g(2)) than in the presence of salt solution (zeta = -2.4 mV, d(LS) =5.3 nm, A(2) = -3.2 x 10(-4) mlmol/g(2)). The M-w strongly depends on the pH and the ionic strength (at pH 3 in the absence of salt, the M-w is 54.6 kDa while in the presence of salt is 114 kDa) which determines the geometry of the protein. The protein-ligand interactions were characterized by fluorescence (FL) and isothermal microcalorimetry (ITC) methods; these independent techniques provided similar thermodynamic parameters such as the binding constant (K) and the Gibbs free energy (Delta G). (C) 2016 Elsevier B.V. All rights reserved. |
|---|---|
| Terjedelem/Fizikai jellemzők: | 51-58 |
| ISSN: | 0141-8130 |